PRDX2_RAT
ID PRDX2_RAT Reviewed; 198 AA.
AC P35704; Q6PDV3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 165.
DE RecName: Full=Peroxiredoxin-2;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P32119};
DE AltName: Full=Thiol-specific antioxidant protein;
DE Short=TSA;
DE AltName: Full=Thioredoxin peroxidase 1;
DE AltName: Full=Thioredoxin-dependent peroxide reductase 1;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000305};
GN Name=Prdx2; Synonyms=Tdpx1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8041738; DOI=10.1073/pnas.91.15.7017;
RA Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.;
RT "Cloning and sequencing of thiol-specific antioxidant from mammalian brain:
RT alkyl hydroperoxide reductase and thiol-specific antioxidant define a large
RT family of antioxidant enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 93-135 AND 140-157, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Might participate in the signaling cascades of growth
CC factors and tumor necrosis factor-alpha by regulating the intracellular
CC concentrations of H(2)O(2). {ECO:0000250|UniProtKB:P32119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:P32119};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer. Interacts with TIPIN.
CC {ECO:0000250|UniProtKB:P32119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
CC -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its
CC condensation to a disulfide bond. It can be reactivated by forming a
CC transient disulfide bond with sulfiredoxin SRXN1, which reduces the
CC cysteine sulfinic acid in an ATP- and Mg-dependent manner.
CC {ECO:0000250|UniProtKB:P32119, ECO:0000250|UniProtKB:Q06830}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P32119}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; U06099; AAA19959.1; -; mRNA.
DR EMBL; BC058481; AAH58481.1; -; mRNA.
DR PIR; A57716; A57716.
DR RefSeq; NP_058865.1; NM_017169.1.
DR RefSeq; XP_006255306.1; XM_006255244.1.
DR AlphaFoldDB; P35704; -.
DR SMR; P35704; -.
DR BioGRID; 247997; 10.
DR IntAct; P35704; 4.
DR MINT; P35704; -.
DR STRING; 10116.ENSRNOP00000004799; -.
DR PeroxiBase; 4477; Rno2CysPrx02.
DR iPTMnet; P35704; -.
DR PhosphoSitePlus; P35704; -.
DR SwissPalm; P35704; -.
DR World-2DPAGE; 0004:P35704; -.
DR jPOST; P35704; -.
DR PaxDb; P35704; -.
DR PRIDE; P35704; -.
DR GeneID; 29338; -.
DR KEGG; rno:29338; -.
DR CTD; 7001; -.
DR RGD; 3838; Prdx2.
DR eggNOG; KOG0852; Eukaryota.
DR InParanoid; P35704; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; P35704; -.
DR TreeFam; TF105181; -.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:P35704; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0002357; P:defense response to tumor cell; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:RGD.
DR GO; GO:0045321; P:leukocyte activation; IBA:GO_Central.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0045581; P:negative regulation of T cell differentiation; ISO:RGD.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; ISO:RGD.
DR GO; GO:0002536; P:respiratory burst involved in inflammatory response; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT CHAIN 2..198
FT /note="Peroxiredoxin-2"
FT /id="PRO_0000135083"
FT DOMAIN 6..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT DISULFID 51
FT /note="Interchain (with C-172); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT DISULFID 172
FT /note="Interchain (with C-51); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P32119"
FT CONFLICT 17
FT /note="G -> A (in Ref. 2; AAH58481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21784 MW; FC6AD9B0E9C4447B CRC64;
MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD
HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN
DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
DTIKPNVDDS KEYFSKHN
